Open AccessCrystallization and preliminary X‐ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus
Author(s) -
Nakasako Masayoshi,
Obata Rika,
Okubo Ryosuke,
Nakayama Shyuichi,
Miyamoto Kenji,
Ohta Hiromichi
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108014723
Subject(s) - orthorhombic crystal system , crystallization , decarboxylation , ammonium sulfate , enantioselective synthesis , molecule , crystallography , chemistry , monomer , stereochemistry , crystal structure , organic chemistry , polymer , catalysis
Arylmalonate decarboxylase catalyses the enantioselective decarboxylation of α‐aryl‐α‐methylmalonates to produce optically pure α‐arylpropionates. The enzyme was crystallized with ammonium sulfate under alkaline pH conditions with the aim of understanding the mechanism of the enantioselective reaction. X‐ray diffraction data collected to a resolution of 3.0 Å at cryogenic temperature showed that the crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 83.13, b = 99.62, c = 139.64 Å. This suggested that the asymmetric unit would contain between four and six molecules. Small‐angle X‐ray scattering revealed that the enzyme exists as a monomer in solution. Thus, the assembly of molecules in the asymmetric unit was likely to have been induced during the crystallization process.